UVRA_LISMO
ID UVRA_LISMO Reviewed; 956 AA.
AC Q8Y4F6;
DT 31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=UvrABC system protein A {ECO:0000255|HAMAP-Rule:MF_00205};
DE Short=UvrA protein {ECO:0000255|HAMAP-Rule:MF_00205};
DE AltName: Full=Excinuclease ABC subunit A {ECO:0000255|HAMAP-Rule:MF_00205};
GN Name=uvrA {ECO:0000255|HAMAP-Rule:MF_00205}; OrderedLocusNames=lmo2488;
OS Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=169963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-679 / EGD-e;
RX PubMed=11679669; DOI=10.1126/science.1063447;
RA Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.-D.,
RA Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W.,
RA Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U.,
RA Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A.,
RA Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B.,
RA Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N.,
RA Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT "Comparative genomics of Listeria species.";
RL Science 294:849-852(2001).
CC -!- FUNCTION: The UvrABC repair system catalyzes the recognition and
CC processing of DNA lesions. UvrA is an ATPase and a DNA-binding protein.
CC A damage recognition complex composed of 2 UvrA and 2 UvrB subunits
CC scans DNA for abnormalities. When the presence of a lesion has been
CC verified by UvrB, the UvrA molecules dissociate. {ECO:0000255|HAMAP-
CC Rule:MF_00205}.
CC -!- SUBUNIT: Forms a heterotetramer with UvrB during the search for
CC lesions. {ECO:0000255|HAMAP-Rule:MF_00205}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00205}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. UvrA family.
CC {ECO:0000255|HAMAP-Rule:MF_00205}.
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DR EMBL; AL591983; CAD00566.1; -; Genomic_DNA.
DR PIR; AH1385; AH1385.
DR RefSeq; NP_466011.1; NC_003210.1.
DR RefSeq; WP_010990003.1; NZ_CP023861.1.
DR AlphaFoldDB; Q8Y4F6; -.
DR SMR; Q8Y4F6; -.
DR STRING; 169963.lmo2488; -.
DR PaxDb; Q8Y4F6; -.
DR EnsemblBacteria; CAD00566; CAD00566; CAD00566.
DR GeneID; 987320; -.
DR KEGG; lmo:lmo2488; -.
DR PATRIC; fig|169963.11.peg.2548; -.
DR eggNOG; COG0178; Bacteria.
DR HOGENOM; CLU_001370_0_2_9; -.
DR OMA; PFEGIIP; -.
DR PhylomeDB; Q8Y4F6; -.
DR BioCyc; LMON169963:LMO2488-MON; -.
DR Proteomes; UP000000817; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0009380; C:excinuclease repair complex; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0009381; F:excinuclease ABC activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006289; P:nucleotide-excision repair; IEA:UniProtKB-UniRule.
DR GO; GO:0009432; P:SOS response; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.1490.20; -; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR HAMAP; MF_00205; UvrA; 1.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR004602; UvrA.
DR InterPro; IPR041552; UvrA_DNA-bd.
DR InterPro; IPR041102; UvrA_inter.
DR Pfam; PF17755; UvrA_DNA-bind; 1.
DR Pfam; PF17760; UvrA_inter; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR TIGRFAMs; TIGR00630; uvra; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 2.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; DNA damage; DNA excision; DNA repair; DNA-binding;
KW Excision nuclease; Metal-binding; Nucleotide-binding; Reference proteome;
KW Repeat; SOS response; Zinc; Zinc-finger.
FT CHAIN 1..956
FT /note="UvrABC system protein A"
FT /id="PRO_0000093062"
FT DOMAIN 309..587
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00205"
FT DOMAIN 607..936
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00205"
FT ZN_FING 252..279
FT /note="C4-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00205"
FT ZN_FING 738..764
FT /note="C4-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00205"
FT BINDING 33..40
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00205"
FT BINDING 639..646
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00205"
SQ SEQUENCE 956 AA; 106482 MW; 43EFEE6CF6D3A0FA CRC64;
MDKEKIVIQG ARAHNLKNID VEIPRDKLVV MTGLSGSGKS SLAFDTIYAE GQRRYVESLS
AYARQFLGQM DKPDVDLIEG LSPAISIDQK TTSRNPRSTV GTVTEIHDYL RLLYARVGHP
VCPNHGIEIT SQTIEQMVDR VLEYPEKTRI QIMAPIVSGK KGTHKKTIEE IKKEGYVRIR
VDGEIYDIND EIEIEKNKKH SIEIIIDRIV IKEGINTRLY DSIEAALRLA DGYAVVDIMG
DKELLFSEHY ACPYCGFSVG ELEPRMFSFN SPFGACPTCD GLGTKLEVDV DTVIPDRSMS
LNEGAIIPWR PISSQYYPQM LASACKEFGI DMDTPLEKLS KEELDIILNG SKDKEFYFEY
KNDFGMTRET WIPFEGILPN IERRYRETNS DFTRDQMAQY MTDLPCPSCK GYRLKEETLS
VKVNDHHIGQ ISEFSINEAL AFFDGLELSE KETQIAAPIF KEVRARLGFL KNVGLDYLTM
SRAAGTLSGG EAQRIRLATQ IGSRLTGVLY ILDEPSIGLH QRDNDRLIST LQSMRDIGNT
LIVVEHDEDT MMAADYLIDI GPGAGEHGGR IVAAGTPEEV ANNKNSITGD YLSGKKFIPV
PAKRRKGNGL ELEIIGAKAN NLKNVNAKIP LATFSCVTGV SGSGKSSLVN EVLRKALARK
LNRNHAKPGE HKEIKGIENL EKIINIDQSP IGRTPRSNPA TYTGAFDDIR DLFASTNEAK
VRGYKKGRFS FNVKGGRCEA CKGDGIIKIE MHFLPDVYVP CEVCHGKRYN GETLDIRYKG
KNIAEVLEMT VEEGLEYFTN QPRIARKLQT IVDVGLGYIR LGQPATTLSG GEAQRVKLAS
ELHKRSNGKS FYILDEPTTG LHADDIGRLL KVLQRLVEEN GDTVLVIEHN LDVIKQADYL
IDLGPEGGDG GGQIIATGTP EKIARSKKSY TGKYLKPILE RDKERTEERI ATAKKK